García-Patrone M, González N S, Algranati I D
Proc Natl Acad Sci U S A. 1971 Nov;68(11):2822-5. doi: 10.1073/pnas.68.11.2822.
The isolation of a new factor, which can cause the in vitro association of 30S and 50S ribosomal subunits at low Mg(++) concentration, is described. The association factor is eluted together with the dissociation protein when ribosomes of Bacillus stearothermophilus are washed with salt solutions of high concentration. The association activity is heat-stable, whereas dissociation factor is inactivated after 10 min at 80 degrees C. This treatment allows the separation of both factors. Several properties rule out the possibility that uncharged, amino-acyl-, or peptidyl-tRNA are responsible for the association process described in this report. Digestion with trypsin shows that the association factor contains at least two components, one of which is a protein.
本文描述了一种新因子的分离,该因子能在低镁离子浓度下导致30S和50S核糖体亚基在体外发生结合。当嗜热脂肪芽孢杆菌的核糖体用高浓度盐溶液洗涤时,结合因子与解离蛋白一起被洗脱。结合活性具有热稳定性,而解离因子在80℃下10分钟后即失活。这种处理方法可将两种因子分离。多项特性排除了无电荷的、氨酰基或肽基 - tRNA参与本报告所述结合过程的可能性。用胰蛋白酶消化表明,结合因子至少包含两个组分,其中之一是一种蛋白质。